Abstract
Hypogastrura harveyi (snow fleas) produce a glycine‐rich antifreeze protein which enables it to survive in environments that would otherwise freeze its body fluid. Snow flea antifreeze protein (sfAFP) is a 6.5 kDa monomeric protein made of six alpha helices linked by hydrogen bonds and disulfide bridges. The protein's amino acid sequence has a frequent glycine‐x‐y amino acid pattern, where the x amino acid is also glycine 50% of the time and the y amino acid is either hydrophobic or hydrophilic. The hydrophobic side of sfAFP binds to the surface of seed ice crystals, breaking up the ice surface into smaller areas and preventing the further binding of water molecules due to the Kelvin effect. Other AFP's have been shown to be efficacious in improving the preservation of rat hearts, leading to the yet‐untested hypothesis that sfAFP's are also able to prolong the cryopreservation of organs. The Ashbury MSOE Center for BioMolecular Modeling SMART Team used 3‐D modeling and printing technology to examine structure‐function relationships of sfAFP when bonding to an ice lattice.Support or Funding InformationMSOE ‐ Center for Biomolecular Modelling ‐ co‐sponsor Diane MunzenmaierThis abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
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